메뉴 건너뛰기




Volumn 287, Issue 10, 2012, Pages 7256-7264

Ubiquitination of human leukocyte antigen (HLA)-DM by different membrane-associated RING-CH (MARCH) protein family E3 ligases targets different endocytic pathways

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN PRESENTING CELLS; CELL SURFACES; CLASS II; CYTOPLASMIC TAIL; ENDOCYTIC MACHINERY; ENDOCYTIC PATHWAYS; HUMAN LEUKOCYTE ANTIGEN; INDUCED LOSS; LIGASES; LYSINE RESIDUES; PEPTIDE LOADING; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN FAMILY; TYROSINE RESIDUES; UBIQUITIN; UBIQUITINATION;

EID: 84857694719     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.305961     Document Type: Article
Times cited : (23)

References (50)
  • 1
    • 0019962031 scopus 로고
    • Membrane insertion and oligomeric assembly of HLA-DR histocompatibility antigens
    • Kvist, S., Wiman, K., Claesson, L., Peterson, P. A., and Dobberstein, B. (1982) Membrane insertion and oligomeric assembly of HLA-DR histocompatibility antigens. Cell 29, 61-69 (Pubitemid 12027672)
    • (1982) Cell , vol.29 , Issue.1 , pp. 61-69
    • Kvist, S.1    Wiman, K.2    Claesson, L.3
  • 2
    • 0026088251 scopus 로고
    • Formation of a nine-subunit complex by HLA class II glycoproteins and the invariant chain
    • Roche, P. A., Marks, M. S., and Cresswell, P. (1991) Formation of a nine-subunit complex by HLA class II glycoproteins and the invariant chain. Nature 354, 392-394 (Pubitemid 21896847)
    • (1991) Nature , vol.354 , Issue.6352 , pp. 392-394
    • Roche, P.A.1    Marks, M.S.2    Cresswell, P.3
  • 3
    • 0027525192 scopus 로고
    • The MHC class II-associated invariant chain contains two endosomal targeting signals within its cytoplasmic tail
    • Pieters, J., Bakke, O., and Dobberstein, B. (1993) The MHC class II-associated invariant chain contains two endosomal targeting signals within its cytoplasmic tail. J. Cell Sci. 106, 831-846 (Pubitemid 23346796)
    • (1993) Journal of Cell Science , vol.106 , Issue.3 , pp. 831-846
    • Pieters, J.1    Bakke, O.2    Dobberstein, B.3
  • 4
    • 0028229612 scopus 로고
    • An LI and ML motif in the cytoplasmic tail of the MHC-associated invariant chain mediate rapid internalization
    • Bremnes, B., Madsen, T., Gedde-Dahl, M., and Bakke, O. (1994) An LI and ML motif in the cytoplasmic tail of the MHC-associated invariant chain mediate rapid internalization. J. Cell Sci. 107, 2021-2032 (Pubitemid 24226451)
    • (1994) Journal of Cell Science , vol.107 , Issue.7 , pp. 2021-2032
    • Bremnes, B.1    Madsen, T.2    Gedde-Dahl, M.3    Bakke, O.4
  • 5
    • 0028350714 scopus 로고
    • An essential role for HLA-DM in antigen presentation by class II major histocompatibility molecules
    • DOI 10.1038/368551a0
    • Morris, P., Shaman, J., Attaya, M., Amaya, M., Goodman, S., Bergman, C., Monaco, J. J., and Mellins, E. (1994) An essential role for HLA-DM in antigen presentation by class II major histocompatibility molecules. Nature 368, 551-554 (Pubitemid 24118772)
    • (1994) Nature , vol.368 , Issue.6471 , pp. 551-554
    • Morris, P.1    Shaman, J.2    Attaya, M.3    Amaya, M.4    Goodman, S.5    Bergman, C.6    Monaco, J.J.7    Mellins, E.8
  • 6
    • 0028518547 scopus 로고
    • Assembly and intracellular transport of HLA-DM and correction of the class II antigen-processing defect in T2 cells
    • Denzin, L. K., Robbins, N. F., Carboy-Newcomb, C., and Cresswell, P. (1994) Assembly and intracellular transport of HLA-DM and correction of the class II antigen-processing defect in T2 cells. Immunity 1, 595-606
    • (1994) Immunity , vol.1 , pp. 595-606
    • Denzin, L.K.1    Robbins, N.F.2    Carboy-Newcomb, C.3    Cresswell, P.4
  • 7
    • 0028676010 scopus 로고
    • In vivo and in vitro formation and dissociation of HLA-DR complexes with invariant chain-derived peptides
    • Avva, R. R., and Cresswell, P. (1994) In vivo and in vitro formation and dissociation of HLA-DR complexes with invariant chain-derived peptides. Immunity 1, 763-774
    • (1994) Immunity , vol.1 , pp. 763-774
    • Avva, R.R.1    Cresswell, P.2
  • 9
    • 0029084023 scopus 로고
    • DM enhances peptide binding to class II MHC by release of invariant chain-derived peptide
    • Sherman, M. A., Weber, D. A., and Jensen, P. E. (1995) DM enhances peptide binding to class II MHC by release of invariant chain-derived peptide. Immunity 3, 197-205
    • (1995) Immunity , vol.3 , pp. 197-205
    • Sherman, M.A.1    Weber, D.A.2    Jensen, P.E.3
  • 10
    • 0029824101 scopus 로고    scopus 로고
    • Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA- DM
    • DOI 10.1126/science.274.5287.618
    • Weber, D. A., Evavold, B. D., and Jensen, P. E. (1996) Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM. Science 274, 618-620 (Pubitemid 26360442)
    • (1996) Science , vol.274 , Issue.5287 , pp. 618-620
    • Weber, D.A.1    Evavold, B.D.2    Jensen, P.E.3
  • 11
    • 0029807634 scopus 로고    scopus 로고
    • Human histocompatibility leukocyte antigen (HLA)-DM edits peptides presented by HLA-DR according to their ligand binding motifs
    • van Ham, S. M., Grüneberg, U., Malcherek, G., Bröker, I., Melms, A., and Trowsdale, J. (1996) Human histocompatibility leukocyte antigen (HLA)-DM edits peptides presented by HLA-DR according to their ligand binding motifs. J. Exp. Med. 184, 2019-2024 (Pubitemid 26404492)
    • (1996) Journal of Experimental Medicine , vol.184 , Issue.5 , pp. 2019-2024
    • Van Ham, S.M.1    Gruneberg, U.2    Malcherek, G.3    Broker, I.4    Melms, A.5    Trowsdale, J.6
  • 13
    • 0030458137 scopus 로고    scopus 로고
    • HLA-DM interactions with intermediates in HLA-DR maturation and a role for HLA-DM in stabilizing empty HLA-DR molecules
    • DOI 10.1084/jem.184.6.2153
    • Denzin, L. K., Hammond, C., and Cresswell, P. (1996) HLA-DM interactions with intermediates in HLA-DR maturation and a role for HLA-DM in stabilizing empty HLA-DR molecules. J. Exp. Med. 184, 2153-2165 (Pubitemid 27023716)
    • (1996) Journal of Experimental Medicine , vol.184 , Issue.6 , pp. 2153-2165
    • Denzin, L.K.1    Hammond, C.2    Cresswell, P.3
  • 14
    • 0028820625 scopus 로고
    • A lysosomal targeting signal in the cytoplasmic tail of the β chain directs HLA-DM to MHC class II compartments
    • Marks, M. S., Roche, P. A., van Donselaar, E., Woodruff, L., Peters, P. J., and Bonifacino, J. S. (1995) A lysosomal targeting signal in the cytoplasmic tail of the β chain directs HLA-DM to MHC class II compartments. J. Cell Biol. 131, 351-369
    • (1995) J. Cell Biol. , vol.131 , pp. 351-369
    • Marks, M.S.1    Roche, P.A.2    Van Donselaar, E.3    Woodruff, L.4    Peters, P.J.5    Bonifacino, J.S.6
  • 15
    • 0030209751 scopus 로고    scopus 로고
    • Targeting signal and subcellular compartments involved in the intracellular trafficking of HLA-DMB
    • Copier, J., Kleijmeer, M. J., Ponnambalam, S., Oorschot, V., Potter, P., Trowsdale, J., and Kelly, A. (1996) Targeting signal and subcellular compartments involved in the intracellular trafficking of HLA-DMB. J. Immunol. 157, 1017-1027
    • (1996) J. Immunol. , vol.157 , pp. 1017-1027
    • Copier, J.1    Kleijmeer, M.J.2    Ponnambalam, S.3    Oorschot, V.4    Potter, P.5    Trowsdale, J.6    Kelly, A.7
  • 16
    • 0025071238 scopus 로고
    • Cycling of cell surface MHC glycoproteins through primaquine-sensitive intracellular compartments
    • Reid, P. A., and Watts, C. (1990) Cycling of cell surface MHC glycoproteins through primaquine-sensitive intracellular compartments. Nature 346, 655-657
    • (1990) Nature , vol.346 , pp. 655-657
    • Reid, P.A.1    Watts, C.2
  • 17
    • 0031046893 scopus 로고    scopus 로고
    • Related leucine-based cytoplasmic targeting signals in invariant chain and major histocompatibility complex class II molecules control endocytic presentation of distinct determinants in a single protein
    • DOI 10.1084/jem.185.3.429
    • Zhong, G., Romagnoli, P., and Germain, R. N. (1997) Related leucine-based cytoplasmic targeting signals in invariant chain and major histocompatibility complex class II molecules control endocytic presentation of distinct determinants in a single protein. J. Exp. Med. 185, 429-438 (Pubitemid 27078361)
    • (1997) Journal of Experimental Medicine , vol.185 , Issue.3 , pp. 429-438
    • Zhong, G.1    Romagnoli, P.2    Germain, R.N.3
  • 18
    • 0025182003 scopus 로고
    • The minimal number of class II MHC-antigen complexes needed for T cell activation
    • Demotz, S., Grey, H. M., and Sette, A. (1990) The minimal number of class II MHC-antigen complexes needed for T cell activation. Science 249, 1028-1030
    • (1990) Science , vol.249 , pp. 1028-1030
    • Demotz, S.1    Grey, H.M.2    Sette, A.3
  • 19
    • 0025286210 scopus 로고
    • Quantitation of antigen-presenting cell MHC class II/peptide complexes necessary for T-cell stimulation
    • Harding, C. V., and Unanue, E. R. (1990) Quantitation of antigen-presenting cell MHC class II/peptide complexes necessary for T-cell stimulation. Nature 346, 574-576
    • (1990) Nature , vol.346 , pp. 574-576
    • Harding, C.V.1    Unanue, E.R.2
  • 20
    • 33750593611 scopus 로고    scopus 로고
    • Surface expression of MHC class II in dendritic cells is controlled by regulated ubiquitination
    • DOI 10.1038/nature05261, PII NATURE05261
    • Shin, J. S., Ebersold, M., Pypaert, M., Delamarre, L., Hartley, A., and Mellman, I. (2006) Surface expression of MHC class II in dendritic cells is controlled by regulated ubiquitination. Nature 444, 115-118 (Pubitemid 44684767)
    • (2006) Nature , vol.444 , Issue.7115 , pp. 115-118
    • Shin, J.-S.1    Ebersold, M.2    Pypaert, M.3    Delamarre, L.4    Hartley, A.5    Mellman, I.6
  • 21
    • 33845397207 scopus 로고    scopus 로고
    • Dendritic Cells Regulate Exposure of MHC Class II at Their Plasma Membrane by Oligoubiquitination
    • DOI 10.1016/j.immuni.2006.11.001, PII S1074761306005164
    • van Niel, G., Wubbolts, R., Ten Broeke, T., Buschow, S. I., Ossendorp, F. A., Melief, C. J., Raposo, G., van Balkom, B. W., and Stoorvogel, W. (2006) Dendritic cells regulate exposure of MHC class II at their plasma membrane by oligoubiquitination. Immunity 25, 885-894 (Pubitemid 44894949)
    • (2006) Immunity , vol.25 , Issue.6 , pp. 885-894
    • Van Niel, G.1    Wubbolts, R.2    Ten, B.T.3    Buschow, S.I.4    Ossendorp, F.A.5    Melief, C.J.6    Raposo, G.7    Van Balkom, B.W.8    Stoorvogel, W.9
  • 25
    • 78650647904 scopus 로고    scopus 로고
    • Dendritic cell activation prevents MHC class II ubiquitination and promotes MHC class II survival regardless of the activation stimulus
    • Walseng, E., Furuta, K., Goldszmid, R. S., Weih, K. A., Sher, A., and Roche, P. A. (2010) Dendritic cell activation prevents MHC class II ubiquitination and promotes MHC class II survival regardless of the activation stimulus. J. Biol. Chem. 285, 41749-41754
    • (2010) J. Biol. Chem. , vol.285 , pp. 41749-41754
    • Walseng, E.1    Furuta, K.2    Goldszmid, R.S.3    Weih, K.A.4    Sher, A.5    Roche, P.A.6
  • 31
    • 0346373729 scopus 로고    scopus 로고
    • Downregulation of Major Histocompatibility Complex Class I by Human Ubiquitin Ligases Related to Viral Immune Evasion Proteins
    • DOI 10.1128/JVI.78.3.1109-1120.2004
    • Bartee, E., Mansouri, M., Hovey Nerenberg, B. T., Gouveia, K., and Früh, K. (2004) Down-regulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins. J. Virol. 78, 1109-1120 (Pubitemid 38095821)
    • (2004) Journal of Virology , vol.78 , Issue.3 , pp. 1109-1120
    • Bartee, E.1    Mansouri, M.2    Nerenberg, B.T.H.3    Gouveia, K.4    Fruh, K.5
  • 32
    • 71049168842 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture and differential plasma membrane proteome quantitation identify new substrates for the MARCH9 transmembrane E3 ligase
    • Hör, S., Ziv, T., Admon, A., and Lehner, P. J. (2009) Stable isotope labeling by amino acids in cell culture and differential plasma membrane proteome quantitation identify new substrates for the MARCH9 transmembrane E3 ligase. Mol. Cell Proteomics 8, 1959-1971
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 1959-1971
    • Hör, S.1    Ziv, T.2    Admon, A.3    Lehner, P.J.4
  • 34
    • 65449174924 scopus 로고    scopus 로고
    • The HLA-DRα chain is modified by polyubiquitination
    • Lapaque, N., Jahnke, M., Trowsdale, J., and Kelly, A. P. (2009) The HLA-DRα chain is modified by polyubiquitination. J. Biol. Chem. 284, 7007-7016
    • (2009) J. Biol. Chem. , vol.284 , pp. 7007-7016
    • Lapaque, N.1    Jahnke, M.2    Trowsdale, J.3    Kelly, A.P.4
  • 36
    • 0032193687 scopus 로고    scopus 로고
    • The tetraspan protein CD82 is a resident of MHC class II compartments where it associates with HLA-DR, -DM, and -DO molecules
    • Hammond, C., Denzin, L. K., Pan, M., Griffith, J. M., Geuze, H. J., and Cresswell, P. (1998) The tetraspan protein CD82 is a resident of MHC class II compartments where it associates with HLA-DR, -DM, and -DO molecules. J. Immunol. 161, 3282-3291
    • (1998) J. Immunol. , vol.161 , pp. 3282-3291
    • Hammond, C.1    Denzin, L.K.2    Pan, M.3    Griffith, J.M.4    Geuze, H.J.5    Cresswell, P.6
  • 37
    • 0026093582 scopus 로고
    • A new human HLA class II-related locus, DM
    • Kelly, A. P., Monaco, J. J., Cho, S. G., and Trowsdale, J. (1991) A new human HLA class II-related locus, DM. Nature 353, 571-573 (Pubitemid 21912559)
    • (1991) Nature , vol.353 , Issue.6344 , pp. 571-573
    • Kelly, A.P.1    Monaco, J.J.2    Cho, S.3    Trowsdale, J.4
  • 38
    • 0030819379 scopus 로고    scopus 로고
    • Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo
    • Zufferey, R., Nagy, D., Mandel, R. J., Naldini, L., and Trono, D. (1997) Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo. Nat. Biotechnol. 15, 871-875
    • (1997) Nat. Biotechnol. , vol.15 , pp. 871-875
    • Zufferey, R.1    Nagy, D.2    Mandel, R.J.3    Naldini, L.4    Trono, D.5
  • 39
    • 77949497792 scopus 로고    scopus 로고
    • Trafficking of MHC class II in dendritic cells is dependent on but not regulated by degradation of its associated invariant chain
    • ten Broeke, T., de Graaff, A., van't Veld, E. M., Wauben, M. H., Stoorvogel, W., and Wubbolts, R. (2010) Trafficking of MHC class II in dendritic cells is dependent on but not regulated by degradation of its associated invariant chain. Traffic 11, 324-331
    • (2010) Traffic , vol.11 , pp. 324-331
    • Ten Broeke, T.1    De Graaff, A.2    Van't Veld, E.M.3    Wauben, M.H.4    Stoorvogel, W.5    Wubbolts, R.6
  • 40
    • 33845907631 scopus 로고    scopus 로고
    • A cost effective non-commercial ECL-solution for Western blot detections yielding strong signals and low background
    • DOI 10.1016/j.jim.2006.07.027, PII S0022175906002948
    • Haan, C., and Behrmann, I. (2007) A cost effective noncommercial ECL solution for Western blot detections yielding strong signals and low background. J. Immunol. Methods 318, 11-19 (Pubitemid 46026809)
    • (2007) Journal of Immunological Methods , vol.318 , Issue.1-2 , pp. 11-19
    • Haan, C.1    Behrmann, I.2
  • 42
    • 21744433861 scopus 로고    scopus 로고
    • Biochemistry: Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase
    • DOI 10.1126/science.1110340
    • Cadwell, K., and Coscoy, L. (2005) Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase. Science 309, 127-130 (Pubitemid 40934990)
    • (2005) Science , vol.309 , Issue.5731 , pp. 127-130
    • Cadwell, K.1    Coscoy, L.2
  • 43
    • 0025402516 scopus 로고
    • Human transferrin receptor internalization is partially dependent upon an aromatic amino acid on the cytoplasmic domain
    • McGraw, T. E., and Maxfield, F. R. (1990) Human transferrin receptor internalization is partially dependent upon an aromatic amino acid on the cytoplasmic domain. Cell Regul. 1, 369-377
    • (1990) Cell Regul. , vol.1 , pp. 369-377
    • McGraw, T.E.1    Maxfield, F.R.2
  • 44
    • 0025990745 scopus 로고
    • Localization of the signal for rapid internalization of the bovine cation-independent mannose 6-phosphate/insulin-like growth factor-II receptor to amino acids 24-29 of the cytoplasmic tail
    • Canfield, W. M., Johnson, K. F., Ye, R. D., Gregory, W., and Kornfeld, S. (1991) Localization of the signal for rapid internalization of the bovine cation-independent mannose 6-phosphate/insulin-like growth factor-II receptor to amino acids 24-29 of the cytoplasmic tail. J. Biol. Chem. 266, 5682-5688 (Pubitemid 21909548)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.9 , pp. 5682-5688
    • Canfield, W.M.1    Johnson, K.F.2    Ye, R.D.3    Gregory, W.4    Kornfeld, S.5
  • 45
    • 0027180886 scopus 로고
    • In vitro binding of plasma membrane-coated vesicle adaptors to the cytoplasmic domain of lysosomal acid phosphatase
    • Sosa, M. A., Schmidt, B., von Figura, K., and Hille-Rehfeld, A. (1993) In vitro binding of plasma membrane-coated vesicle adaptors to the cytoplasmic domain of lysosomal acid phosphatase. J. Biol. Chem. 268, 12537-12543 (Pubitemid 23182413)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.17 , pp. 12537-12543
    • Sosa, M.A.1    Schmidt, B.2    Von Figura, K.3    Hille-Rehfeld, A.4
  • 46
    • 0033620656 scopus 로고    scopus 로고
    • Molecular bases for the recognition of tyrosine-based sorting signals
    • DOI 10.1083/jcb.145.5.923
    • Bonifacino, J. S., and Dell'Angelica, E. C. (1999) Molecular bases for the recognition of tyrosine-based sorting signals. J. Cell Biol. 145, 923-926 (Pubitemid 29270051)
    • (1999) Journal of Cell Biology , vol.145 , Issue.5 , pp. 923-926
    • Bonifacino, J.S.1    Dell'Angelica, E.C.2
  • 48
    • 34547115036 scopus 로고    scopus 로고
    • The ubiquitin ligase SCF(βTrCP) regulates the degradation of the growth hormone receptor
    • DOI 10.1074/jbc.M702610200
    • van Kerkhof, P., Putters, J., and Strous, G. J. (2007) The ubiquitin ligase SCF(βTrCP) regulates the degradation of the growth hormone receptor. J. Biol. Chem. 282, 20475-20483 (Pubitemid 47099991)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.28 , pp. 20475-20483
    • Van Kerkhof, P.1    Putters, J.2    Strous, G.J.3
  • 49
    • 1842556279 scopus 로고    scopus 로고
    • Adaptable adaptors for coated vesicles
    • Robinson, M. S. (2004) Adaptable adaptors for coated vesicles. Trends Cell Biol. 14, 167-174
    • (2004) Trends Cell Biol. , vol.14 , pp. 167-174
    • Robinson, M.S.1
  • 50
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • Raiborg, C., and Stenmark, H. (2009) The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 458, 445-452
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.